ID A0A1G4FIS4_9FIRM Unreviewed; 1099 AA.
AC A0A1G4FIS4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=pcrA_1 {ECO:0000313|EMBL:SCL86491.1};
GN ORFNames=PP176A_1095 {ECO:0000313|EMBL:SCL86491.1};
OS Sporanaerobacter sp. PP17-6a.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC Sporanaerobacter.
OX NCBI_TaxID=1891289 {ECO:0000313|EMBL:SCL86491.1, ECO:0000313|Proteomes:UP000179042};
RN [1] {ECO:0000313|EMBL:SCL86491.1, ECO:0000313|Proteomes:UP000179042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP176A {ECO:0000313|EMBL:SCL86491.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; FMIF01000010; SCL86491.1; -; Genomic_DNA.
DR RefSeq; WP_071139431.1; NZ_FMIF01000010.1.
DR AlphaFoldDB; A0A1G4FIS4; -.
DR Proteomes; UP000179042; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd19067; PfuEndoQ-like; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:SCL86491.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:SCL86491.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000179042}.
FT DOMAIN 469..731
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 732..1011
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 425..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1099 AA; 124953 MW; B6C637EA6AA22893 CRC64;
MFIADFHIHS KYSRATSKEC IPEILEMWSR RKGINLLGTA DFTHPVWREE LKEKLTPSEE
GLYVLKDDYR KEDNIGGTDF KPRFIISGEI SSIYKKNGKV RKIHNLILLP GLEEAELISH
RLEAIGNLHS DGRPILGLDS KDLLEIVLDI CPEAIFIPAH IWTPHFSLYG EYSGFDDIRE
CFKDLTDNIY AVETGLSSDP PMNWRLSALD KFTLVSNSDA HSPANLAREA NIFDTDLSYS
NISQALKNRN TKEFYGTIEF FPEEGKYHYD GHRNCKVCLK PAETEALSGI CPVCGGRLTV
GVLHRVEALA DRAEGFVPQT AKHFESLVPL REIIASSLGF TTASIKVKRR YENLIQTLGT
ELFILREASL SDIELAAGPH IAEGIRRLRA GQVEIHPGYD GKYGQINVMN KNEINLISGQ
ISLFKNEDNN DRNNDKNNDI QKQSLIKKER VSEPYSASSI EPLPSSNPYR LNQEQWEDVS
SPEPVIVVMA GPGTGKTRTL VYRIVYLIEN CGISPSEITA VTFTNKAANE MRSRLEKHFK
NKNTVKAMNI GTFHSICLKI LSEEKGNGKT TIIDEYNSIS IVEDILKNLQ LKISPRDAMK
EISLMKSGTI SGEENKKELK IPLEVYDLYC SQLKQYDVMD YDDILLEALK KFKNTNLSNS
FSYLLVDEFQ DINEIQYRLI KEWASNNIFV IGDPEQSIYG FRGSDFRYFD IFKENFPHAK
NIRLIQNYRS TPEIIHCAKS VISKKIKGEP FSFLESKREK GTKVRLLKTN NEFSEALFVA
KEINRIVGGI DMIDTQKISE TDRKNSKVKN PRSFADIAIL YRTNHQANII EQCLIKEGIP
YVVAGKDEFL SEKEVRAVIA FFQFLLNPKD IFSLKTYLKI SGIYSTELIQ EILKNYVSAK
KNIPSLIKII EKVQPSDDLV KSWNFIELLK KYEPLLHKEK PVKLIDSWIN DNNLSGIDCL
KLLLNTSVFH NNMPSFIQTL ILGHESDVVR SSSKIYSSDA VSLMTIHGSK GLEFPVIFIC
GVNDGLIPLK NSGRDFNLDE ERRLFYVGMT RAQDELILIT SHDRPSPFIS DIPEDSIIKE
NTSTNKHRPQ SKQLSIFDI
//